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    The amino acid sequence of cytosolic aspartate aminotransferase from human liver

    Doyle, Sean and Schininà, M.E. and Bossa, F. and Doonan, S. (1990) The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochemical Journal, 270 (3). pp. 651-657. ISSN 0264-6021

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    1. The cytosolic aspartate aminotransferase was purified from human liver. 2. The isoenzyme contains four cysteine residues, only one of which reacts with 5,5′-dithiobis-(2-nitrobenzoic acid) in the absence of denaturing agents. 3. The amino acid sequence of the isoenzyme is reported, as determined from peptides produced by digestion with trypsin and with CNBr, and from sub-digestion of some of these peptides with Staphylococcus aureus V8 proteinase. 4. The isoenzyme shares 48% identity of amino acid sequence with the mitochondrial form from human heart. 5. Comparisons of the amino acid sequences of all known mammalian cytosolic aspartate aminotransferases and of the same set of mitochondrial isoenzymes are reported. The results indicate that the cytosolic isoenzymes have evolved at about 1.3 times the rate of the mitochondrial forms. 6. The time elapsed since the cytosolic and mitochondrial isoenzymes diverged from a common ancestral protein is estimated to be 860 x 10(6) years. 7. Experimental details and confirmatory data for the results presented here are given in a supplementary paper that has been deposited as a Supplementary Publication SUP 50158 (25 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J.

    Item Type: Article
    Keywords: amino acid sequence; cytosolic aspartate aminotransferase; human liver;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 7411
    Identification Number:
    Depositing User: Dr. Sean Doyle
    Date Deposited: 30 Aug 2016 14:19
    Journal or Publication Title: Biochemical Journal
    Publisher: Portland Press
    Refereed: Yes
    Use Licence: This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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